Ong S H, Goh K C, Lim Y P, Low B C, Klint P, Claesson-Welsh L, Cao X, Tan Y H, Guy G R
Signal Transduction Laboratory, National University of Singapore, Republic of Singapore.
Biochem Biophys Res Commun. 1996 Aug 23;225(3):1021-6. doi: 10.1006/bbrc.1996.1288.
In Swiss 3T3 fibroblasts, basic fibroblast growth factor (bFGF) stimulates the unique tyrosine phosphorylation of a protein complex around 90 kDa, as ascertained by high resolution 2-D PAGE and anti-phosphotyrosine blotting. The majority of this complex consists of the protein(s) designated previously as SNT (suc1-associated neurotrophic factor target). Tyrosine phosphorylated SNT binds to both p13suc1 protein and the SH2 domain of Grb2. Binding of SNT to Grb2 is likely to be mediated through the consensus binding motif, pYXN, on SNT. The binding of SNT to p13suc1 is independent of the pYXN motif. Tyrosine phosphorylated SNT is localised in the plasma membrane where it could form a complex with Grb2 and Sos, enabling the initiation of a novel FGF-specific signalling pathway.
在瑞士3T3成纤维细胞中,碱性成纤维细胞生长因子(bFGF)刺激一种约90 kDa的蛋白质复合物发生独特的酪氨酸磷酸化,这是通过高分辨率二维聚丙烯酰胺凝胶电泳(2-D PAGE)和抗磷酸酪氨酸印迹法确定的。该复合物的大部分由先前指定为SNT(与suc1相关的神经营养因子靶点)的蛋白质组成。酪氨酸磷酸化的SNT与p13suc1蛋白和Grb2的SH2结构域都结合。SNT与Grb2的结合可能是通过SNT上的共有结合基序pYXN介导的。SNT与p13suc1的结合不依赖于pYXN基序。酪氨酸磷酸化的SNT定位于质膜,在那里它可以与Grb2和Sos形成复合物,从而启动一条新的FGF特异性信号通路。